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Kinetic Study of the Interaction of Oxy- and Deoxyhemoglobins with the Erythrocyte Membrane

Overview
Journal Proc Natl Acad Sci U S A
Specialty Science
Date 1980 Dec 1
PMID 6938961
Citations 4
Authors
N Shaklai
V S Sharma
Affiliations
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Abstract

Changes in fluorescence intensity of a membrane-embedded probe were used to study the kinetics of binding of oxy- and deoxyhemoglobin to erythrocyte membranes. For these studies, stopped-flow fluorimetric techniques were utilized. Both binding and dissociation of hemoglobin from membranes followed heterogeneous first-order kinetics. The rate constants for binding of oxyhemoglobin were about 10 times larger than those of deoxyhemoglobin; the dissociation rate constants of oxyhemoglobin were about one-quarter those of the unliganded form. The results are discussed in light of the steady-state binding constants previously derived for both oxy- and deoxyhemoglobin.

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